Crystallization and preliminary X-ray diffraction analysis of human IL-22 bound to the extracellular IL-22R1 chain.
作者信息
Jones Brandi C, Logsdon Naomi J, Walter Mark R
机构信息
Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Apr 1;64(Pt 4):266-9. doi: 10.1107/S1744309108004752. Epub 2008 Mar 21.
Abstract
Interleukin-22 (IL-22) is a potent mediator of cellular inflammatory responses. Crystals of IL-22 bound to the extracellular high-affinity cell-surface receptor sIL-22R1 have been grown from polyethylene glycol solutions. Crystals suitable for X-ray diffraction analysis were only obtained with mutants of IL-22 and sIL-22R1 that removed the N-linked glycosylation sites found in the wild-type amino-acid sequences. The crystals belonged to space group P2(1), with unit-cell parameters a = 50.43, b = 76.33, c = 114.92 A, beta = 92.45 degrees , and diffracted X-rays to 3.2 A resolution. The crystallographic asymmetric unit contained two IL-22-sIL-22R1 complexes, corresponding to a solvent content of approximately 52%.
摘要
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